P20618 (PSB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit beta type-1
EC=3.4.25.1

Alternative name(s):
Macropain subunit C5
Multicatalytic endopeptidase complex subunit C5
Proteasome component C5
Proteasome gamma chain

Gene names

Name:	PSMB1
Synonyms:	PSC5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with SERPINB2. Interacts with HIV-1 TAT protein. Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the peptidase T1B family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome antigen processing and presentation of peptide antigen via MHC class I Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome protein polyubiquitination Traceable author statement. Source: Reactome regulation of apoptotic process Traceable author statement. Source: Reactome regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PSMB7	Q99436	6	EBI-372273,EBI-603319

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 28	28			PRO_0000259623
	Chain	29 – 241	213	Proteasome subunit beta type-1		PRO_0000148030
Amino acid modifications
	Modified residue	150	1	Phosphotyrosine By similarity
	Modified residue	204	1	N6-acetyllysine Ref.10
Natural variations
	Natural variant	11	1	P → A. Ref.5 Corresponds to variant rs12717 [ dbSNP | Ensembl ].		VAR_051547
	Natural variant	208	1	I → N. Corresponds to variant rs10541 [ dbSNP | Ensembl ].		VAR_051548

Sequences

	Sequence		Length	Mass (Da)
	P20618 [UniParc]. Last modified May 1, 1992. Version 2. Checksum: AE8FC42799F39157	FASTA	241	26,489
	10 20 30 40 50 60 MLSSTAMYSA PGRDLGMEPH RAAGPLQLRF SPYVFNGGTI LAIAGEDFAI VASDTRLSEG 70 80 90 100 110 120 FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL KMYKHSNNKA MTTGAIAAML 130 140 150 160 170 180 STILYSRRFF PYYVYNIIGG LDEEGKGAVY SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ 190 200 210 220 230 240 VGFKNMQNVE HVPLSLDRAM RLVKDVFISA AERDVYTGDA LRICIVTKEG IREETVSLRK D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)." Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A. Biochim. Biophys. Acta 1089:95-102(1991) [PubMed: 2025653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-11. Tissue: Brain and Lung.
[6]	"Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)." Lee L.W., Moomaw C.R., Orth K., McGuire M.J., DeMartino G.N., Slaughter C.A. Biochim. Biophys. Acta 1037:178-185(1990) [PubMed: 2306472] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-52.
[7]	"Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits." Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E. FEBS Lett. 553:200-204(2003) [PubMed: 14550573] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[8]	"Interaction of plasminogen activator inhibitor-2 and proteasome subunit, beta type 1." Fan J., Zhang Y.Q., Li P., Hou M., Tan L., Wang X., Zhu Y.S. Acta Biochim. Biophys. Sin. 36:42-46(2004) [PubMed: 14732874] [Abstract] Cited for: INTERACTION WITH SERPINB2.
[9]	"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex." Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L. Biochemistry 46:3553-3565(2007) [PubMed: 17323924] [Abstract] Cited for: PROTEOLYTIC PROCESSING [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204, MASS SPECTROMETRY.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00761 mRNA. Translation: BAA00658.1. BT019720 mRNA. Translation: AAV38525.1. AB451312 mRNA. Translation: BAG70126.1. AB451442 mRNA. Translation: BAG70256.1. AL031259 Genomic DNA. Translation: CAA20287.1. BC000508 mRNA. Translation: AAH00508.1. BC020807 mRNA. Translation: AAH20807.1.
IPI	IPI00025019.
PIR	SNHUC5. S15973.
RefSeq	NP_002784.1. NM_002793.3.
UniGene	Hs.352768.
3D structure databases
ProteinModelPortal	P20618.
SMR	P20618. Positions 29-241.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20618. 14 interactions.
MINT	MINT-3009312.
STRING	P20618.
Protein family/group databases
MEROPS	T01.986.
PTM databases
PhosphoSite	P20618.
Polymorphism databases
DMDM	130853.
2D gel databases
REPRODUCTION-2DPAGE	IPI00025019.
UCD-2DPAGE	P20618.
Proteomic databases
PeptideAtlas	P20618.
PRIDE	P20618.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262193; ENSP00000262193; ENSG00000008018.
GeneID	5689.
KEGG	hsa:5689.
UCSC	uc003qxr.1. human.
Organism-specific databases
CTD	5689.
GeneCards	GC06M170761.
H-InvDB	HIX0006400.
HGNC	HGNC:9537. PSMB1.
HPA	CAB033911. HPA029635. HPA029637.
MIM	602017. gene.
neXtProt	NX_P20618.
PharmGKB	PA33882.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16614.
HOGENOM	HBG318170.
HOVERGEN	HBG000961.
InParanoid	P20618.
OMA	SYEREQC.
OrthoDB	EOG4PG61P.
PhylomeDB	P20618.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_13505. Proteasome mediated degradation of PAK-2p34. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	P20618.
Bgee	P20618.
CleanEx	HS_PSMB1.
Genevestigator	P20618.
GermOnline	ENSG00000008018. Homo sapiens.
Family and domain databases
InterPro	IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
KO	K02732.
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00188. Bortezomib.
NextBio	22098.
SOURCE	Search...

Entry information

Entry name

PSB1_HUMAN

Accession

Primary (citable) accession number: P20618
Secondary accession number(s): B5BU76, Q9BWA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	May 1, 1992
Last modified:	January 25, 2012
This is version 132 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.